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References from Leveraging structure-informed machine learning for fast steric zipper propensity prediction across whole proteomes. Local targets link to admitted publications; unresolved targets remain external evidence.
Erratum: The amyloid state and its association with protein misfolding diseases
10.1038/nrm3826 · 2014 · External reference
Functional amyloid--from bacteria to humans
10.1016/j.tibs.2007.03.003 · 2007 · External reference
The expanding amyloid family: Structure, stability, function, and pathogenesis
10.1016/j.cell.2021.08.013 · 2021 · External reference
The X-ray interpretation of denaturation and the structure of the seed globulins
10.1042/bj0292351 · 1935 · External reference
Common core structure of amyloid fibrils by synchrotron X-ray diffraction
10.1006/jmbi.1997.1348 · 1997 · External reference
Atomic structures of amyloid cross-beta spines reveal varied steric zippers
10.1038/nature05695 · 2007 · External reference
Rnq1: An epigenetic modifier of protein function in yeast
10.1016/s1097-2765(00)80412-8 · 2000 · External reference
A systematic survey identifies prions and illuminates sequence features of prionogenic proteins
10.1016/j.cell.2009.02.044 · 2009 · External reference
Identifying the amylome, proteins capable of forming amyloid-like fibrils
10.1073/pnas.0915166107 · 2010 · External reference
Unresolved reference
2021 · External reference
Molecular interactions of FG nucleoporin repeats at high resolution
10.1038/s41557-022-01035-7 · 2022 · External reference
Screening for amyloid proteins in the yeast proteome
10.1007/s00294-017-0759-7 · 2018 · External reference
Accurate structure prediction of biomolecular interactions with AlphaFold 3
10.1038/s41586-024-07487-w · 2024 · External reference
Unresolved reference
2024 · External reference
Structure of the cross-beta spine of amyloid-like fibrils
10.1038/nature03680 · 2005 · External reference
The activities of amyloids from a structural perspective
10.1038/nature20416 · 2016 · External reference
Structural Studies of Amyloid Proteins at the Molecular Level
10.1146/annurev-biochem-061516-045104 · 2017 · External reference
The 3D profile method for identifying fibril-forming segments of proteins
10.1073/pnas.0511295103 · 2006 · External reference
The hydrophobin EAS is largely unstructured in solution and functions by forming amyloid-like structures
10.1016/s0969-2126(00)00559-1 · 2001 · External reference
Structural and functional role of the disulfide bridges in the hydrophobin SC3
10.1074/jbc.m000691200 · 2000 · External reference
Self-assembly of functional, amphipathic amyloid monolayers by the fungal hydrophobin EAS
10.1073/pnas.1114052109 · 2012 · External reference
A novel class of secreted hydrophobic proteins is involved in aerial hyphae formation in Streptomyces coelicolor by forming amyloid-like fibrils
10.1101/gad.264303 · 2003 · External reference
Role of Escherichia coli curli operons in directing amyloid fiber formation
10.1126/science.1067484 · 2002 · External reference
Structural predictions of AgfA, the insoluble fimbrial subunit of Salmonella thin aggregative fimbriae
10.1006/jmbi.1999.2882 · 1999 · External reference
Amyloid adhesins are abundant in natural biofilms
10.1111/j.1462-2920.2007.01418.x · 2007 · External reference
Widespread abundance of functional bacterial amyloid in mycolata and other gram-positive bacteria
10.1128/aem.02107-08 · 2009 · External reference
Cold-shock induction of a family of TIP1-related proteins associated with the membrane in Saccharomyces cerevisiae
10.1111/j.1365-2958.1995.tb02248.x · 1995 · External reference
Correlation of structural elements and infectivity of the HET-s prion
10.1038/nature03793 · 2005 · External reference
Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core
10.1126/science.1151839 · 2008 · External reference
Structural analysis and architectural principles of the bacterial amyloid curli
10.1038/s41467-023-38204-2 · 2023 · External reference
Modeling Pseudomonas syringae ice-nucleation protein as a beta-helical protein
10.1016/s0006-3495(01)76093-6 · 2001 · External reference
Novel dimeric β-helical model of an ice nucleation protein with bridged active sites
10.1186/1472-6807-11-36 · 2011 · External reference
Ice nucleation proteins self-assemble into large fibres to trigger freezing at near 0 °C
10.7554/elife.91976 · 2023 · External reference
Luminidependens (LD) is an Arabidopsis protein with prion behavior
10.1073/pnas.1604478113 · 2016 · External reference
Thermostability and aliphatic index of globular proteins
1980 · External reference
Correlation between stability of a protein and its dipeptide composition: a novel approach for predicting in vivo stability of a protein from its primary sequence
10.1093/protein/4.2.155 · 1990 · External reference
A simple method for displaying the hydropathic character of a protein
10.1016/0022-2836(82)90515-0 · 1982 · External reference
